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Database: UniProt
Entry: C8XPN3_TECDE
LinkDB: C8XPN3_TECDE
Original site: C8XPN3_TECDE 
ID   C8XPN3_TECDE            Unreviewed;       394 AA.
AC   C8XPN3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE            EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
DE   Flags: Fragment;
GN   Name=atpB {ECO:0000313|EMBL:ABU93554.1};
OS   Tectaria devexa (Fern).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ABU93554.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Polypodiineae; Tectariaceae;
OC   Tectaria.
OX   NCBI_TaxID=65713 {ECO:0000313|EMBL:ABU93554.1};
RN   [1] {ECO:0000313|EMBL:ABU93554.1}
RP   NUCLEOTIDE SEQUENCE.
RX   AGRICOLA=IND43981165; DOI=10.1086/521710;
RA   Liu H.-M., Zhang X.-C., Wang W., Qiu Y.-L., Chen Z.-D.;
RT   "Molecular phylogeny of the fern family Dryopteridaceae inferred from
RT   chloroplast rbcL and atpB genes.";
RL   Int. J. Plant Sci. 168:1311-1323(2007).
RN   [2] {ECO:0000313|EMBL:ABU93554.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Liu H., Zhang X., Chen Z., Qiu Y.;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The catalytic sites are hosted primarily by the
CC       beta subunits. {ECO:0000256|ARBA:ARBA00037290}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001741,
CC         ECO:0000256|RuleBase:RU003553};
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main
CC       subunits: a(1), b(1), b'(1) and c(9-12).
CC       {ECO:0000256|RuleBase:RU003553}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; EF450520; ABU93554.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8XPN3; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR   CDD; cd01133; F1-ATPase_beta_CD; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01039; atpD; 1.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW   ECO:0000256|RuleBase:RU003553};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW   Chloroplast {ECO:0000313|EMBL:ABU93554.1};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003553}; Plastid {ECO:0000313|EMBL:ABU93554.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          93..285
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABU93554.1"
FT   NON_TER         394
FT                   /evidence="ECO:0000313|EMBL:ABU93554.1"
SQ   SEQUENCE   394 AA;  42226 MW;  D2ADBA58BA5283DE CRC64;
     TEVRAVAMSA TDGLMRGMGA VDTGAPLSVP VGETTLGRIS NVLGEPVDNL GPVRSSATFP
     IHRSAPPFTQ LDTKLSIFET GIKVVDLLAP YRRGGKIGLF GGAGVGKTVP ITESINNIAK
     AHGGVSVSGG VGERTREGND LYMEMKESKV INEQNISESK VALVYGQMNE PPGARMRVGS
     TALTMAEYFR DVNKQDVLLF IDHIFRFVQA GSEVSALLGR MPSAVGYQPT LGTEMGSLQE
     RITSTKEGSI TSIQAVYVPA DDLTDPAPAT TSAHLDATTV LSRGLAAKGI YPAVDPLDST
     STMLQPWIVG EEHYETAQGV KQTLQRYKEL QDIIAILGLD ELSEEDRLTV ARARKIERFL
     SQPFFVAEVF TGSPGKYVSL SETIKGFQMI LSGE
//
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